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Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

The growth of white-rot fungus Pleurotus eryngii F032 in a suitable medium can degrade an azo dye Reactive Black 5 (RB5), because of its ability to produce ligninolytic enzymes such as lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase that able to degrade and transform the complex str...

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Published in:Water, air, and soil pollution air, and soil pollution, 2013-06, Vol.224 (6), p.1-9, Article 1595
Main Authors: Hadibarata, Tony, Adnan, Liyana Amalina, Yusoff, Abdull Rahim Mohd, Yuniarto, Adhi, Rubiyatno, Zubir, Meor Mohd Fikri Ahmad, Khudhair, Ameer Badr, Teh, Zee Chuang, Naser, M. Abu
Format: Article
Language:English
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Summary:The growth of white-rot fungus Pleurotus eryngii F032 in a suitable medium can degrade an azo dye Reactive Black 5 (RB5), because of its ability to produce ligninolytic enzymes such as lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase that able to degrade and transform the complex structure of the dye into a less toxic compound. The effect of environmental factors such as initial concentration of Reactive Black 5, pH, temperature of growth medium, surfactant (Tween 80), and agitation were also investigated. The productions of ligninolytic enzymes were enhanced by increasing the white-rot fungi growth in optimum conditions. The decolorization of Reactive Black 5 were analyzed by using UV–vis spectrophotometer at the maximum absorbance of 596 nm. The white-rot fungus, P. eryngii F032 culture exhibited 93.56 % decolorization of 10 mg/L RB5 within 72 h of incubation in dark condition with agitation. The optimum pH and temperature for the decolorizing activity was recorded at pH 3 and 40 °C, respectively. The addition of surfactant (Tween 80) increased the decolorization to 93.57 % and agitation of growth medium at 120 rpm enhanced the distribution of nutrients to the fungus thus optimized the enzymatic reaction that resulted maximum decolorization of RB5 which was 93.57 %. The molecular docking studies were performed using Chimera visualization software as to analyze the decolorization mechanism of RB5 at molecular level.
ISSN:0049-6979
1573-2932
DOI:10.1007/s11270-013-1595-0